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Topic · Enzyme inhibition

The principle

To identify inhibition type, compare how the inhibitor changes $K_{m}$ and $V_{m a x}$ .

Work

v = \frac{V _{m a x} [ S ]}{K _{m} + [ S ]}

For competitive inhibition:

K_{m, app} = K_{m} (1 + \frac{[ I ]}{K _{i}})

$V_{m a x}$ stays the same.

The inhibitor competes for the active site, so more substrate is needed to reach half of $V_{m a x}$ .

At high $[S]$ , substrate can outcompete the inhibitor, so $V_{m a x}$ does not change.

Trap

Do not assume every inhibitor lowers $V_{m a x}$ .

Why this trap is tempting

Students remember "inhibitor lowers activity" and jump to lower $V_{m a x}$ . But competitive inhibition mainly affects apparent substrate affinity, so $K_{m}$ increases while $V_{m a x}$ stays the same.

Takeaway

For inhibition questions, ask: did $K_{m}$ , $V_{m a x}$ , or both change?

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